ID   PCDB3_PANTR             Reviewed;         796 AA.
AC   Q5DRD1;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Protocadherin beta-3;
DE            Short=PCDH-beta-3;
DE   Flags: Precursor;
GN   Name=PCDHB3;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=15744052; DOI=10.1534/genetics.104.037606;
RA   Wu Q.;
RT   "Comparative genomics and diversifying selection of the clustered
RT   vertebrate protocadherin genes.";
RL   Genetics 169:2179-2188(2005).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC       involved in the establishment and maintenance of specific neuronal
CC       connections in the brain.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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DR   RefSeq; NP_001013026.1; NM_001013008.2.
DR   AlphaFoldDB; Q5DRD1; -.
DR   SMR; Q5DRD1; -.
DR   STRING; 9598.ENSPTRP00000029632; -.
DR   PaxDb; Q5DRD1; -.
DR   GeneID; 462128; -.
DR   KEGG; ptr:462128; -.
DR   CTD; 56132; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   HOGENOM; CLU_006480_3_0_1; -.
DR   InParanoid; Q5DRD1; -.
DR   OrthoDB; 300321at2759; -.
DR   TreeFam; TF332299; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProt.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR032455; Cadherin_C.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF16492; Cadherin_C_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; SSF49313; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   3: Inferred from homology;
KW   Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..796
FT                   /note="Protocadherin beta-3"
FT                   /id="PRO_0000003919"
FT   TOPO_DOM        27..690
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        691..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        712..796
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..133
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          138..242
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          247..347
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          352..451
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          456..561
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          568..671
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   796 AA;  86773 MW;  15EDF0DC44297901 CRC64;
     MEAGGERFLR QRQVLLLFVF LGGSLAGSES RRYSVAEEKE RGFLIANLAK DLGLRVEELA
     ARGAQVVSKG NKQHFQLSHQ TGDLLLNEKL DREELCGPTE PCILHFQILL QNPLQFVTNE
     LRIIDVNDHS PVFFENEMHL KILESTLPGT VIPLGNAEDL DVGRNSLQNY TITPNSHFHV
     LTRSRRDGRK YPELVLDKAL DREEQPELSL TLTALDGGSP PRSGTAQINI QVLDINDNAP
     EFAQPLYEVA VLENTPVYSV IVTVSASDLD TGSFGTISYA FFHASEEIRK TFQLNPITGD
     MQLVKYLNFE AINSYEVDIE AKDGGGLSGK STVIVQVVDV NDNPPELTLS SVNSPIPENS
     GETVLAVFSV SDLDSGDNGR VMCSIENNLP FFLKPSVENF YTLVSEGALD RETRSEYNIT
     ITITDLGTPR LKTKYNITVL VSDVNDNAPA FTQTSYTLFV RENNSPALHI GSVSATDRDS
     GTNAQVTYSL LPPQDPHLPL SSLVSINADN GHLFALRSLD YEALQAFEFR VGATDRGSPA
     LSSEALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
     WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDAAKHKL AVLVKDNGEP PRSATATLHV
     LLVDGFSQPY LPLPEAAPAQ AQADLLTVYL VVALASVSSL FLFSVLLFVA VRLCRRSRAA
     SVGRCSVPEG PFPGHLVDVS GTGTLSQSYQ YEVCLTGGSG TNEFKFLKPI IPNFVAQGAE
     RVSEANPSFR KSFEFS